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  • Adams, E. (1954) The enzymatic synthesis of histidine from histidinol. J Biol Chem 209: 829846.
  • Alderwick, L.J., Dover, L.G., Seidel, M., Gande, R., Sahm, H., Eggeling, L., and Besra, G.S. (2006) Arabinan-deficient mutants of Corynebacterium glutamicum and the consequent flux in decaprenylmonophosphoryl-d-arabinose metabolism. Glycobiology 16: 10731081.
  • Alifano, P., Piscitelli, C., Blasi, V., Rivellini, F., Nappo, A.G., Bruni, C.B., and Carlomagno, M.S. (1992) Processing of a polycistronic mRNA requires a 5′ cis element and active translation. Mol Microbiol 6: 787798.
  • Alifano, P., Fani, R., Lió, P., Lazcano, A., Bazzicalupo, M., Carlomagno, M.S., and Bruni, C.B. (1996) Histidine biosynthetic pathway and genes: structure, regulation, and evolution. Microbiol Rev 60: 4469.
  • Amaro, R.E., Myers, R.S., Davisson, V.J., and Luthey-Schulten, Z.A. (2005) Structural elements in IGP synthase exclude water to optimize ammonia transfer. Biophys J 89: 475487.
  • Ames, G.F., and Roth, J.R. (1968) Histidine and aromatic permeases of Salmonella typhimurim. J Bacteriol 96: 17421749.
  • Araki, K., and Nakayama, K. (1971) Studies on histidine fermentation: Part I. l-histidine production by histidine analog-resistant mutants from several bacteria. Agric Biol Chem 35: 20812088.
  • Araki, K., and Nakayama, K. (1974) Feedback-resistant phosphoribosyl-ATP pyrophosphorylase in l-histidine-producing mutants of Corynebacterium glutamicum. Agric Biol Chem 38: 22092218.
  • Avarbock, D., Salem, J., Li, L.-S., Wang, Z.M., and Rubin, H. (1999) Cloning and characterization of a bifunctional RelA/SpoT homologue from Mycobacterium tuberculosis. Gene 233: 261269.
  • Barbosa, J.A.R.G., Sivaraman, J., Li, Y., Larocque, R., Matte, A., Schrag, J.D., and Cygler, M. (2002) Mechanism of action and NAD+-binding mode revealed by the crystal structure of l-histidinol dehydrogenase. Proc Natl Acad Sci USA 99: 18591864.
  • Becker, J., and Wittmann, C. (2011) Systems and synthetic metabolic engineering for amino acid production – the heartbeat of industrial strain development. Curr Opin Biotechnol 23: 19.
  • Becker, J., and Wittmann, C. (2012) Bio-based production of chemicals, materials and fuels – Corynebacterium glutamicum as versatile cell factory. Curr Opin Biotechnol 23: 631640.
  • Becker, J., Zelder, O., Hafner, S., Schroder, H., and Wittmann, C. (2011) From zero to hero – design-based systems metabolic engineering of Corynebacterium glutamicum for l-lysine production. Metab Eng 13: 159168.
  • Bellmann, A., Vrljic, M., Pátek, M., Sahm, H., Krämer, R., and Eggeling, L. (2001) Expression control and specificity of the basic amino acid exporter LysE of Corynebacterium glutamicum. Microbiology 147: 17651774.
  • Blombach, B., and Seibold, G.M. (2010) Carbohydrate metabolism in Corynebacterium glutamicum and applications for the metabolic engineering of l-lysine production strains. Appl Microbiol Biotechnol 86: 13131322.
  • Blombach, B., Riester, T., Wieschalka, S., Ziert, C., Youn, J.W., Wendisch, V.F., and Eikmanns, B.J. (2011) Corynebacterium glutamicum tailored for efficient isobutanol production. Appl Environ Microbiol 77: 33003310.
  • Bond, J.P., and Francklyn, C. (2000) Proteobacterial histidine-biosynthetic pathways are paraphyletic. J Mol Evol 50: 339347.
  • Brenner, M., and Ames, B.N. (1971) The histidine operon and its regulation. In Metabolic Pathways. Greenberg, D.M. (ed.). New York, USA: Academic Press, pp. 349387.
  • Brilli, M., and Fani, R. (2004) Molecular evolution of hisB genes. J Mol Evol 58: 225237.
  • Brinkrolf, K., Schröder, J., Pühler, A., and Tauch, A. (2010) The transcriptional regulatory repertoire of Corynebacterium glutamicum: reconstruction of the network controlling pathways involved in lysine and glutamate production. J Biotechnol 149: 173182.
  • Brockmann-Gretza, O., and Kalinowski, J. (2006) Global gene expression during stringent response in Corynebacterium glutamicum in presence and absence of the rel gene encoding (p)ppGpp synthase. BMC Genomics 7: 230.
  • Bröer, S., and Krämer, R. (1991) Lysine excretion by Corynebacterium glutamicum: 1. Identification of a specific secretion carrier system. Eur J Biochem 202: 131135.
  • Camus, J.C., Pryor, M.J., Medigue, C., and Cole, S.T. (2002) Re-annotation of the genome sequence of Mycobacterium tuberculosis H37Rv. Microbiology 148: 29672973.
  • Carlomagno, M.S., Chiariotti, L., Alifano, P., Nappo, A.G., and Bruni, C.B. (1988) Structure and function of the Salmonella typhimurium and Escherichia coli K-12 histidine operons. J Mol Biol 203: 585606.
  • Cashel, M. (1975) Regulation of bacterial ppGpp and pppGpp. Annu Rev Microbiol 29: 301318.
  • Chapman, L.F., and Nester, E.W. (1969) Gene-enzyme relationships in histidine biosynthesis in Bacillus subtilis. J Bacteriol 97: 14441448.
  • Chatterji, D., and Ojha, A.K. (2001) Revisiting the stringent response, ppGpp and starvation signaling. Curr Opin Microbiol 4: 160165.
  • Cho, Y., Sharma, V., and Sacchettini, J.C. (2003) Crystal structure of ATP phosphoribosyltransferase from Mycobacterium tuberculosis. J Biol Chem 278: 83338339.
  • le Coq, D., Fillinger, S., and Aymerich, S. (1999) Histidinol phosphate phosphatase, catalyzing the penultimate step of the histidine biosynthesis pathway, is encoded by ytvP (hisJ) in Bacillus subtilis. J Bacteriol 181: 32773280.
  • Crawford, I.P., and Eberly, L. (1986) Structure and regulation of the anthranilate synthase genes in Pseudomonas aeruginosa: I. Sequence of trpG encoding the glutamine amidotransferase subunit. Mol Biol Evol 3: 436448.
  • Due, A.V., Kuper, J., Geerlof, A., Kries, J.P., and Wilmanns, M. (2011) Bisubstrate specificity in histidine/tryptophan biosynthesis isomerase from Mycobacterium tuberculosis by active site metamorphosis. Proc Natl Acad Sci USA 108: 35543559.
  • Eccleston, E.D., Thayer, M.L., and Kirkwood, S. (1979) Mechanisms of action of histidinol dehydrogenase and UDP-Glc dehydrogenase: evidence that the half-reactions proceed on separate subunits. J Biol Chem 254: 1139911404.
  • Eggeling, L. , and Bott, M. (eds). (2005) Handbook of Corynebacterium glutamicum. Boca Raton, FL, USA: Taylor & Francis.
  • Eggeling, L., and Sahm, H. (2003) New ubiquitous translocators: amino acid export by Corynebacterium glutamicum and Escherichia coli. Arch Microbiol 180: 155160.
  • Erdmann, A., Weil, B., and Krämer, R. (1993) Lysine secretion by wild-type Corynebacterium glutamicum triggered by dipeptide uptake. J Gen Microbiol 139: 31153122.
  • Fani, R., Brilli, M., Fondi, M., and Lió, P. (2007) The role of gene fusions in the evolution of metabolic pathways: the histidine biosynthesis case. BMC Evol Biol 7: S4.
  • Fink, G.R. (1964) Gene-enzyme relations in histidine biosynthesis in yeast. Science 146: 525527.
  • Fink, G.R., and Martin, R.G. (1967) Translation and polarity in the histidine operon II: polarity in the histidine operon. J Mol Biol 30: 97107.
  • Gao, B., and Gupta, R.S. (2012) Phylogenetic framework and molecular signatures for the main clades of the phylum Actinobacteria. Microbiol Mol Biol Rev 76: 66112.
  • Garavaglia, M., Rossi, E., Landini, P., and Marinus, M.G. (2012) The pyrimidine nucleotide biosynthetic pathway modulates production of biofilm determinants in Escherichia coli. PLoS ONE 7: e31252.
  • Goodfellow, M., Kämpfer, P., Busse, H.-J., Trujillo, M.E., Suzuki, K.-I., Ludwig, W., and Whitman, W.B. (2012) Bergey's Manual® of Systematic Bacteriology: Volume Five The Actinobacteria, Part A. New York, USA: Springer.
  • Görisch, H., and Hölke, W. (1985) Binding of histidinal to histidinol dehydrogenase. Eur J Biochem 150: 305308.
  • Grisolia, V., Riccio, A., and Bruni, C.B. (1983) Structure and function of the internal promoter (hisBp) of the Escherichia coli K-12 histidine operon. J Bacteriol 155: 12881296.
  • Grubmeyer, C., Skiadopoulos, M., and Senior, A.E. (1989) l-Histidinol dehydrogenase, a Zn2+-metalloenzyme. Arch Biochem Biophys 272: 311317.
  • Gutierrez-Preciado, A., Henkin, T.M., Grundy, F.J., Yanofsky, C., and Merino, E. (2009) Biochemical features and functional implications of the RNA-based T-box regulatory mechanism. Microbiol Mol Biol Rev 73: 3661.
  • Hartman, P.E., Loper, J.C., and Serman, D. (1960) Fine structure mapping by complete transduction between histidine-requiring Salmonella mutants. J Gen Microbiol 22: 323353.
  • Hashimoto, K.I., Murata, J., Konishi, T., Yabe, I., Nakamatsu, T., and Kawasaki, H. (2012) Glutamate is excreted across the cytoplasmic membrane through the NCgl1221 channel of Corynebacterium glutamicum by passive diffusion. Biosci Biotechnol Biochem 76: 14221424.
  • Heery, D.M., and Dunican, L.K. (1993) Cloning of the trp gene cluster from a tryptophan-hyperproducing strain of Corynebacterium glutamicum: identification of a mutation in the trp leader sequence. Appl Environ Microbiol 59: 791799.
  • Henkin, T.M. (1994) tRNA-directed transcription antitermination. Mol Microbiol 13: 381387.
  • Houston, L.L. (1973a) Purification and properties of a mutant bifunctional enzyme from the hisB gene of Salmonella typhimurium. J Biol Chem 248: 41444149.
  • Houston, L.L. (1973b) Specialized subregions of the bifunctional hisB gene of Salmonella typhimurium. J Bacteriol 113: 8287.
  • Huffman, J.L., and Brennan, R.G. (2002) Prokaryotic transcription regulators: more than just the helix-turn-helix motif. Curr Opin Struct Biol 12: 98106.
  • Ikeda, M. (2003) Amino acid production processes. Adv Biochem Eng Biotechnol 79: 135.
  • Ikeda, M., and Nakagawa, S. (2003) The Corynebacterium glutamicum genome: features and impacts on biotechnological processes. Appl Microbiol Biotechnol 62: 99109.
  • Jain, V., Kumar, M., and Chatterji, D. (2006) ppGpp: stringent response and survival. J Microbiol 44: 110.
  • Javid-Majd, F., Yang, D., Ioerger, T.R., and Sacchettini, J.C. (2008) The 1.25 Å resolution structure of phosphoribosyl-ATP pyrophosphohydrolase from Mycobacterium tuberculosis. Acta Crystallogr D Biol Crystallogr 64: 627635.
  • Johnston, H.M., Barnes, W.M., Chumley, F.G., Bossi, L., and Roth, J.R. (1980) Model for regulation of the histidine operon of Salmonella. Proc Natl Acad Sci USA 77: 508512.
  • Jung, S., Chun, J.Y., Yim, S.-H., Lee, S.-S., Cheon, C.-I., Song, E., and Lee, M.-S. (2010) Transcriptional regulation of histidine biosynthesis genes in Corynebacterium glutamicum. Can J Microbiol 56: 178187.
  • Jung, S.-I., Han, M.S., Kwon, J.H., Cheon, C.-I., Min, K.H., and Lee, M.-S. (1998) Cloning of the histidine biosynthetic genes of Corynebacterium glutamicum: organization and sequencing analysis of the hisA, impA, and hisF gene cluster. Biochem Biophys Res Commun 247: 741745.
  • Jung, S.-I., Chun, J.Y., Yim, S.-H., Cheon, C.-I., Song, E., Lee, S.-S., and Lee, M.-S. (2009) Organization and analysis of the histidine biosynthetic genes from Corynebacterium glutamicum. Genes Genom 31: 315323.
  • Kalinowski, J., Bathe, B., Bartels, D., Bischoff, N., Bott, M., Burkovski, A., et al. (2003) The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of l-aspartate-derived amino acids and vitamins. J Biotechnol 104: 525.
  • Kasai, T. (1974) Regulation of the expression of the histidine operon in Salmonella typhimurium. Nature 249: 523527.
  • Kim, J., and Lee, M.-S. (2001) Molecular cloning and analysis of the hisH gene encoding glutamine amidotransferase from Corynebacterium glutamicum. Korean J Genet 23: 121127.
  • Kinoshita, S., Nakayama, S., and Akita, S. (1958) Taxonomic study of glutamic acid accumulating bacteria, Micrococcus glutamicus, nov. sp. Bull Agric Chem Soc Jpn 22: 176185.
  • Klem, T.J., and Davisson, V.J. (1993) Imidazole glycerol phosphate synthase: the glutamine amidotransferase in histidine biosynthesis. Biochemistry 32: 51775186.
  • Klem, T.J., Chen, Y., and Davisson, V.J. (2001) Subunit interactions and glutamine utilization by Escherichia coli imidazole glycerol phosphate synthase. J Bacteriol 183: 989996.
  • Klungsöyr, L., and Kryvi, H. (1971) Sedimentation behaviour of phosphoribosyladenosine triphosphate synthetase: effects of substrates and modifiers. Biochim Biophys Acta 227: 327336.
  • Kuenzler, M., Balmelli, T., Egli, C.M., Paravicini, G., and Braus, G.H. (1993) Cloning, primary structure, and regulation of the HIS7 gene encoding a bifunctional glutamine amidotransferase:cyclase from Saccharomyces cerevisiae. J Bacteriol 175: 55485558.
  • Kwon, J.H., Chun, J.Y., Lee, H.S., Cheon, C.-I., Song, E.-S., Min, K.H., and Lee, M.-S. (2000) Cloning of the histidine biosynthetic genes from Corynebacterium glutamicum: organization and analysis of the hisG and hisE genes. Can J Microbiol 46: 848855.
  • Laffler, T., and Gallant, J. (1974) spoT, a new genetic locus involved in the stringent response in E. coli. Cell 1: 2730.
  • Lee, H.S., Cho, Y., Lee, J.-H., and Kang, S.G. (2008) Novel monofunctional histidinol-phosphate phosphatase of the DDDD superfamily of phosphohydrolases. J Bacteriol 190: 26292632.
  • Litsanov, B., Brocker, M., and Bott, M. (2012) Toward homosuccinate fermentation: metabolic engineering of Corynebacterium glutamicum for anaerobic production of succinate from glucose and formate. Appl Environ Microbiol 78: 33253337.
  • Lohkamp, B., McDermott, G., Campbell, S.A., Coggins, J.R., and Lapthorn, A.J. (2004) The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition. J Mol Biol 336: 131144.
  • Loper, J.C. (1961) Enzyme complementation in mixed extracts of mutants from the Salmonella histidine B locus. Proc Natl Acad Sci USA 47: 14401450.
  • McHardy, A.C., Tauch, A., Rückert, C., Pühler, A., and Kalinowski, J. (2003) Genome-based analysis of biosynthetic aminotransferase genes of Corynebacterium glutamicum. J Biotechnol 104: 229240.
  • Marchler-Bauer, A., Lu, S., Anderson, J.B., Chitsaz, F., Derbyshire, M.K., DeWeese-Scott, C., et al. (2010) CDD: a Conserved Domain Database for the functional annotation of proteins. Nucleic Acids Res 39: D225D229.
  • Marienhagen, J., Kennerknecht, N., Sahm, H., and Eggeling, L. (2005) Functional analysis of all aminotransferase proteins inferred from the genome sequence of Corynebacterium glutamicum. J Bacteriol 187: 76397646.
  • Marienhagen, J., Sandalova, T., Sahm, H., Eggeling, L., and Schneider, G. (2008) Insights into the structural basis of substrate recognition by histidinol-phosphate aminotransferase from Corynebacterium glutamicum. Acta Crystallogr D Biol Crystallogr 64: 675685.
  • Martin, R.G. (1963a) The first enzyme in histidine biosynthesis: the nature of feedback inhibition by histidine. J Biol Chem 238: 257268.
  • Martin, R.G. (1963b) The one operon-one messenger theory of transcription. Cold Spring Harb Symp Quant Biol 28: 357361.
  • Martin, R.G., Berberich, M.A., Ames, B.N., Davis, W.W., Goldberger, R.F., and Yourno, J.D. (1971) [147] Enzymes and intermediates of histidine biosynthesis in Salmonella typhimurium. In Methods in Enzymology: Metabolism of Amino Acids and Amines Part B. Tabor, H. , and Tabor, C.W. (eds). New York, USA: Academic Press, pp. 344.
  • Mizukami, T., Hamu, A., Ikeda, M., Oka, T., and Katsumata, R. (1994) Cloning of the ATP phosphoribosyl transferase gene of Corynebacterium glutamicum and application of the gene to l-histidine production. Biosci Biotechnol Biochem 58: 635638.
  • Mormann, S., Lömker, A., Rückert, C., Gaigalat, L., Tauch, A., Pühler, A., and Kalinowski, J. (2006) Random mutagenesis in Corynebacterium glutamicum ATCC 13032 using an IS6100-based transposon vector identified the last unknown gene in the histidine biosynthesis pathway. BMC Genomics 7: 205.
  • Morton, D.P., and Parsons, S.M. (1977a) Inhibition of ATP phosphoribosyltransferase by AMP and ADP in the absence and presence of histidine. Arch Biochem Biophys 181: 643648.
  • Morton, D.P., and Parsons, S.M. (1977b) Synergistic inhibition of ATP phosphoribosyltransferase by guanosine tetraphosphate and histidine. Biochem Biophys Res Commun 74: 172177.
  • Nasir, N., Vyas, R., Chugh, C., Ahangar, M.S., and Biswal, B.K. (2012) Molecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosis. Acta Crystallogr F 68: 3236.
  • Nelson, D.L., and Cox, M.M. (2009) Lehninger Biochemie. Berlin, Germany: Springer.
  • di Nocera, P.P., Blasi, F., Lauro, R., Frunzio, R., and Bruni, C.B. (1978) Nucleotide sequence of the attenuator region of the histidine operon of Escherichia coli K-12. Proc Natl Acad Sci USA 75: 42764280.
  • Nunes, J.E.S., Ducati, R.G., Breda, A., Rosado, L.A., de Souza, B.M., Palma, M.S., et al. (2011) Molecular, kinetic, thermodynamic, and structural analyses of Mycobacterium tuberculosis hisD-encoded metal-dependent dimeric histidinol dehydrogenase (EC 1.1.1.23). Arch Biochem Biophys 512: 143153.
  • Pátek, M., and Nešvera, J. (2011) Sigma factors and promoters in Corynebacterium glutamicum. J Biotechnol 154: 101113.
  • Polgár, L. (2005) The catalytic triad of serine peptidases. Cell Mol Life Sci 62: 21612172.
  • Rangarajan, E.S., Proteau, A., Wagner, J., Hung, M.-N., Matte, A., and Cygler, M. (2006) Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway. J Biol Chem 281: 3793037941.
  • Rebek, J. (1990) On the structure of histidine and its role in enzyme active sites. Struct Chem 1: 129131.
  • Sawada, K., Zen-in, S., Wada, M., and Yokota, A. (2010) Metabolic changes in a pyruvate kinase gene deletion mutant of Corynebacterium glutamicum ATCC 13032. Metab Eng 12: 401407.
  • Schmid, M.B., and Roth, J.R. (1983) Internal promoters of the his operon in Salmonella typhimurium. J Bacteriol 153: 11141119.
  • Schröder, J., Maus, I., Meyer, K., Wördemann, S., Blom, J., Jaenicke, S., et al. (2012) Complete genome sequence, lifestyle, and multi-drug resistance of the human pathogen Corynebacterium resistens DSM 45100 isolated from blood samples of a leukemia patient. BMC Genomics 13: 141.
  • Seliverstov, A.V., Putzer, H., Gelfand, M.S., and Lyubetsky, V.A. (2005) Comparative analysis of RNA regulatory elements of amino acid metabolism genes in Actinobacteria. BMC Microbiol 5: 54.
  • Sissler, M., Delorme, C., Bond, J., Ehrlich, S.D., Renault, P., and Francklyn, C. (1999) An aminoacyl-tRNA synthetase paralog with a catalytic role in histidine biosynthesis. Proc Natl Acad Sci USA 96: 89858990.
  • Smith, D.W., and Ames, B.N. (1964) Intermediates in the early steps of histidine biosynthesis. J Biol Chem 239: 18481855.
  • Sprenger, G.A. (2007) Aromatic amino acids. In Amino Acid Biosynthesis – Pathways, Regulation and Metabolic Engineering. Wendisch, V.F. (ed.). Berlin, Germany: Springer, pp. 93127.
  • Stepansky, A., and Leustek, T. (2006) Histidine biosynthesis in plants. Amino Acids 30: 127142.
  • Stephens, J.C., Artz, S.W., and Ames, B.N. (1975) Guanosine 5′-diphosphate 3′-diphosphate (ppGpp): positive effector for histidine operon transcription and general signal for amino-acid deficiency. Proc Natl Acad Sci USA 72: 43894393.
  • Stolz, M., Peters-Wendisch, P., Etterich, H., Gerharz, T., Faurie, R., Sahm, H., et al. (2007) Reduced folate supply as a key to enhanced l-serine production by Corynebacterium glutamicum. Appl Environ Microbiol 73: 750755.
  • Struhl, K., and Davis, R.W. (1977) Production of a functional eukaryotic enzyme in Escherichia coli: cloning and expression of the yeast structural gene for imidazole-glycerolphosphate dehydratase (his3). Proc Natl Acad Sci USA 74: 52555259.
  • Tauch, A., Wehmeier, L., Götker, S., Pühler, A., and Kalinowski, J. (2001) Relaxed rrn expression and amino acid requirement of a Corynebacterium glutamicum rel mutant defective in (p)ppGpp metabolism. FEMS Microbiol Lett 201: 5358.
  • Tébar, A.R., Fernández, V.M., MartinDelRío, R., and Ballesteros, A.O. (1973) Studies on the quaternary structure of the first enzyme for histidine biosynthesis. Experientia 29: 14771479.
  • Tosa, T., and Pizer, L.I. (1971) Biochemical bases for the antimetabolite action of l-serine hydroxamate. J Bacteriol 106: 972982.
  • Vasicová, P., Pátek, M., Nešvera, J., Sahm, H., and Eikmanns, B. (1999) Analysis of the Corynebacterium glutamicum dapA promoter. J Bacteriol 181: 61886191.
  • Viswanathan, V.K., Green, J.M., and Nichols, B.P. (1995) Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli. J Bacteriol 177: 59185923.
  • Vitreschak, A.G., Mironov, A.A., Lyubetsky, V.A., and Gelfand, M.S. (2008) Comparative genomic analysis of T-box regulatory systems in bacteria. RNA 14: 717735.
  • Wehmeier, L., Schäfer, A., Burkovski, A., Krämer, R., Mechold, U., Malke, H., et al. (1998) The role of the Corynebacterium glutamicum rel gene in (p)ppGpp metabolism. Microbiology 144: 18531862.
  • Wehrmann, A., Morakkabati, S., Krämer, R., Sahm, H., and Eggeling, L. (1995) Functional analysis of sequences adjacent to dapE of Corynebacterium glutamicum reveals the presence of aroP, which encodes the aromatic amino acid transporter. J Bacteriol 177: 59915993.
  • Wendisch, V.F. (ed.). (2007) Amino Acid Biosynthesis – Pathways, Regulation and Metabolic Engineering. Berlin, Germany: Springer.
  • Winkler, M. (1996) Biosynthesis of histidine. In Escherichia coli and Salmonella: Cellular and Molecular Biology. Neidhardt, F.C. (ed.). Washington, DC, USA: ASM Press, pp. 485505.
  • Yoo, J.-H., and RajBhandary, U.L. (2008) Requirements for translation re-initiation in Escherichia coli: roles of initiator tRNA and initiation factors IF2 and IF3. Mol Microbiol 67: 10121026.
  • Yoshida, K.-I., Sano, H., Seki, S., Oda, M., Fujimura, M., and Fujita, Y. (1995) Cloning and sequencing of a 29 kb region of the Bacillus subtilis genome containing the hut and wapA loci. Microbiology 141: 337343.
  • Zhang, Y., Morar, M., and Ealick, S.E. (2008) Structural biology of the purine biosynthetic pathway. Cell Mol Life Sci 65: 36993724.
  • Zhang, Y., Shang, X., Deng, A., Chai, X., Lai, S., Zhang, G., and Wen, T. (2012) Genetic and biochemical characterization of Corynebacterium glutamicum ATP phosphoribosyltransferase and its three mutants resistant to feedback inhibition by histidine. Biochimie 94: 829838.
  • Zhao, Z., Ding, J.-Y., Li, T., Zhou, N.-Y., and Liu, S.-J. (2011) The ncgl1108 (phePCg) gene encodes a new l-phe transporter in Corynebacterium glutamicum. Appl Microbiol Biotechnol 90: 20052013.
  • Zhao, Z., Ding, J.-Y., Ma, W.-H., Zhou, N.-Y., and Liu, S.-J. (2012) Identification and characterization of γ-aminobutyric acid uptake system GabPCg (NCgl0464) in Corynebacterium glutamicum. Appl Environ Microbiol 78: 25962601.
  • Zheng, X., Hu, G.-Q., She, Z.-S., and Zhu, H. (2011) Leaderless genes in bacteria: clue to the evolution of translation initiation mechanisms in prokaryotes. BMC Genomics 12: 361.